Description
Antipain is a protease inhibitor originally isolated from actinomycetes. It inhibits thrombokinase, plasmin, trypsin, and papain in vitro (IC50s = 20, 93, 0.26, and 0.16 μg/ml, respectively). Antipain (6-600 μg/ml) inhibits the morphological transformation of and increases frequency of chromosomal aberrations in Syrian hamster embryo cells induced by N-methyl-N''-nitro-N-nitroso-guanidine (MNNG). In vivo, antipain (25-100 mg/kg) suppresses urethan-induced formation of cleft palates and cleft lips in mice.
Uses
Concentrations for 50% inhibition (μg/ml): papain, 0.16trypsin, 0.26cathepsin A, 1.19cathepsin B, 0.59cathepsin D, 125plasmin, >93chymotrypsin and pepsin, >250It also has been reported to inhibit calpain I, (porcine) with Ki = 1.4 μM
General Description
Antipain is a protease inhibitor isolated from actinomycetes. It inhibits thrombokinase and blood coagulation.
Biochem/physiol Actions
Reversible inhibitor of serine/cysteine proteases and some trypsin-like serine proteases. Its action resembles leupeptin; however, its plasmin inhibition is less and its cathepsin A inhibition is more than that observed with leupeptin. Chronic administration of antipain can reduce the frequency of chemically induced transformation in BALB/c-/3T3 cells.
References
1) Umezawa?et al.?(1976),?Structures and activities of protease inhibitors of microbial origin; Method Enzymol.,?45?678
2) Gotoh?et al.?(2001),?Proteolytic activity and recombinant protein production in virus-infected Sf-9 insect cell cultures supplemented with carboxyl and cysteine protease inhibitors; J. Biosci. Bioeng.,?92?248
3) Hockensmith?et al. (2016), Identification and characterization of a chymotrypsin-like serine protease from periodontal pathogen, Tannerella forsythia; Microb. Pathog.,?100?37
4) Mat Amin?et al. (2004),?Proteinases in Naegleria Fowleri (strain NF3), a pathogenic amoeba: a preliminary study.; Trop. Biomed.,?21?57
5) Moriyyasu & Inoue (2008),?Use of protease inhibitor for detecting autophagy in plants; Methods Enzymol.,?451?557